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Protein

Ras-related protein Rab-9B

Gene

RAB9B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the transport of proteins between the endosomes and the trans Golgi network.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi14 – 229GTP
Nucleotide bindingi62 – 665GTP
Nucleotide bindingi124 – 1274GTP
Nucleotide bindingi154 – 1563GTP

GO - Molecular functioni

  1. GDP binding Source: UniProtKB
  2. GTPase activity Source: GO_Central
  3. GTP binding Source: GO_Central

GO - Biological processi

  1. GTP catabolic process Source: GO_Central
  2. intracellular protein transport Source: GO_Central
  3. Rab protein signal transduction Source: GO_Central
  4. retrograde transport, endosome to Golgi Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-9B
Alternative name(s):
Rab-9-like protein
Short name:
Rab-9L
Gene namesi
Name:RAB9B
Synonyms:RAB9L
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:14090. RAB9B.

Subcellular locationi

Cell membrane Curated; Lipid-anchor Curated; Cytoplasmic side Curated. Cytoplasmic vesiclephagosome 1 Publication. Cytoplasmic vesiclephagosome membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity
Note: Recruited to phagosomes containing S.aureus or M.tuberculosis.

GO - Cellular componenti

  1. late endosome Source: GO_Central
  2. lysosome Source: GO_Central
  3. phagocytic vesicle Source: UniProtKB
  4. phagocytic vesicle membrane Source: UniProtKB-SubCell
  5. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34153.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 201201Ras-related protein Rab-9BPRO_0000121142Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi200 – 2001S-geranylgeranyl cysteineBy similarity
Lipidationi201 – 2011S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Lipoprotein, Prenylation

Proteomic databases

MaxQBiQ9NP90.
PaxDbiQ9NP90.
PRIDEiQ9NP90.

PTM databases

PhosphoSiteiQ9NP90.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ9NP90.
CleanExiHS_RAB9B.
GenevestigatoriQ9NP90.

Organism-specific databases

HPAiHPA061932.

Interactioni

Protein-protein interaction databases

BioGridi119382. 10 interactions.
IntActiQ9NP90. 1 interaction.
STRINGi9606.ENSP00000243298.

Structurei

Secondary structure

1
201
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 138Combined sources
Helixi20 – 2910Combined sources
Beta strandi41 – 5313Combined sources
Beta strandi55 – 639Combined sources
Helixi67 – 693Combined sources
Helixi70 – 734Combined sources
Helixi74 – 763Combined sources
Beta strandi81 – 888Combined sources
Helixi92 – 965Combined sources
Helixi98 – 10811Combined sources
Turni114 – 1163Combined sources
Beta strandi119 – 1246Combined sources
Helixi135 – 14410Combined sources
Beta strandi150 – 1523Combined sources
Turni155 – 1584Combined sources
Helixi161 – 17313Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OCBX-ray2.20A2-180[»]
ProteinModelPortaliQ9NP90.
SMRiQ9NP90. Positions 3-175.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NP90.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi36 – 449Effector regionBy similarity

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000119125.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiQ9NP90.
KOiK07900.
OMAiKEFMYYS.
OrthoDBiEOG7G4QG8.
PhylomeDBiQ9NP90.
TreeFamiTF326442.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9NP90-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSGKSLLLKV ILLGDGGVGK SSLMNRYVTN KFDSQAFHTI GVEFLNRDLE
60 70 80 90 100
VDGRFVTLQI WDTAGQERFK SLRTPFYRGA DCCLLTFSVD DRQSFENLGN
110 120 130 140 150
WQKEFIYYAD VKDPEHFPFV VLGNKVDKED RQVTTEEAQT WCMENGDYPY
160 170 180 190 200
LETSAKDDTN VTVAFEEAVR QVLAVEEQLE HCMLGHTIDL NSGSKAGSSC

C
Length:201
Mass (Da):22,719
Last modified:October 1, 2000 - v1
Checksum:iB35EDA8E8358C49C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB036693 mRNA. Translation: BAA89542.1.
AK313425 mRNA. Translation: BAG36217.1.
AL139228 Genomic DNA. Translation: CAB76967.1.
BC093756 mRNA. Translation: AAH93756.1.
BC093758 mRNA. Translation: AAH93758.1.
CCDSiCCDS14515.1.
RefSeqiNP_057454.1. NM_016370.2.
XP_006724721.1. XM_006724658.1.
XP_006724722.1. XM_006724659.1.
UniGeneiHs.522736.

Genome annotation databases

EnsembliENST00000243298; ENSP00000243298; ENSG00000123570.
GeneIDi51209.
KEGGihsa:51209.
UCSCiuc004ell.2. human.

Polymorphism databases

DMDMi13124471.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB036693 mRNA. Translation: BAA89542.1.
AK313425 mRNA. Translation: BAG36217.1.
AL139228 Genomic DNA. Translation: CAB76967.1.
BC093756 mRNA. Translation: AAH93756.1.
BC093758 mRNA. Translation: AAH93758.1.
CCDSiCCDS14515.1.
RefSeqiNP_057454.1. NM_016370.2.
XP_006724721.1. XM_006724658.1.
XP_006724722.1. XM_006724659.1.
UniGeneiHs.522736.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OCBX-ray2.20A2-180[»]
ProteinModelPortaliQ9NP90.
SMRiQ9NP90. Positions 3-175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119382. 10 interactions.
IntActiQ9NP90. 1 interaction.
STRINGi9606.ENSP00000243298.

PTM databases

PhosphoSiteiQ9NP90.

Polymorphism databases

DMDMi13124471.

Proteomic databases

MaxQBiQ9NP90.
PaxDbiQ9NP90.
PRIDEiQ9NP90.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000243298; ENSP00000243298; ENSG00000123570.
GeneIDi51209.
KEGGihsa:51209.
UCSCiuc004ell.2. human.

Organism-specific databases

CTDi51209.
GeneCardsiGC0XM103077.
HGNCiHGNC:14090. RAB9B.
HPAiHPA061932.
MIMi300285. gene.
neXtProtiNX_Q9NP90.
PharmGKBiPA34153.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000119125.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiQ9NP90.
KOiK07900.
OMAiKEFMYYS.
OrthoDBiEOG7G4QG8.
PhylomeDBiQ9NP90.
TreeFamiTF326442.

Miscellaneous databases

EvolutionaryTraceiQ9NP90.
GenomeRNAii51209.
NextBioi54280.
PROiQ9NP90.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NP90.
CleanExiHS_RAB9B.
GenevestigatoriQ9NP90.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning of a new member of the Ras superfamily, RAB9-like, on the human chromosome Xq22.1-q22.3 region."
    Seki N., Azuma T., Yoshikawa T., Masuho Y., Muramatsu M., Saito T.
    J. Hum. Genet. 45:318-322(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Cerebellum.
  3. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  5. "Rab GTPases regulating phagosome maturation are differentially recruited to mycobacterial phagosomes."
    Seto S., Tsujimura K., Koide Y.
    Traffic 12:407-420(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  6. "Crystal structure of human RAB9B in complex with a GTP analogue."
    Structural genomics consortium (SGC)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 2-180 IN COMPLEX WITH GTP ANALOG.

Entry informationi

Entry nameiRAB9B_HUMAN
AccessioniPrimary (citable) accession number: Q9NP90
Secondary accession number(s): B2R8M0, Q52LX2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: October 1, 2000
Last modified: February 4, 2015
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.